Appearance of a nonfunctional isozyme of hepatic glycogen synthase in late gestation.

Autor: Hsu SD; Department of Anatomy and Cell Biology, University of Cincinnati, Ohio., Jaspers SR, Davis BB, Cardell RR Jr, Miller TB Jr, Drake RL
Jazyk: angličtina
Zdroj: Archives of biochemistry and biophysics [Arch Biochem Biophys] 1990 Aug 15; Vol. 281 (1), pp. 152-6.
DOI: 10.1016/0003-9861(90)90425-x
Abstrakt: Glycogen levels, glycogen synthase activities, and glycogen synthase protein levels were determined in liver tissues obtained from 14- to 19-day-old fetal mice, newborn mice, and adult mice. The results of these experiments demonstrate a significant increase in the quantity of hepatic glycogen synthase beginning at Day 17 of gestation and reaching adult levels at birth. However, during the same time period, there is a dramatic decrease in total glycogen synthase activity suggesting that the accumulating glycogen synthase molecules are unable to transfer UDP-glucose to glycogen. These inversely coordinated changes in the quantity and activity of glycogen synthase are consistent with the suggestion that glycogen synthesis in the near-term fetal mouse is being maintained by preexisting enzyme, while accumulating enzyme molecules may represent a quiescent isozyme.
Databáze: MEDLINE